ID IL17F_HUMAN Reviewed; 163 AA. AC Q96PD4; Q6NSI0; Q7Z6P4; Q96PI8; Q9NUE6; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 3. DT 24-JAN-2024, entry version 176. DE RecName: Full=Interleukin-17F; DE Short=IL-17F; DE AltName: Full=Cytokine ML-1; DE Flags: Precursor; GN Name=IL17F; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=11591732; DOI=10.4049/jimmunol.167.8.4137; RA Starnes T., Robertson M.J., Sledge G., Kelich S., Nakshatri H., RA Broxmeyer H.E., Hromas R.; RT "IL-17F, a novel cytokine selectively expressed in activated T cells and RT monocytes, regulates angiogenesis and endothelial cell cytokine RT production."; RL J. Immunol. 167:4137-4140(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-161. RC TISSUE=Blood; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-163, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=11591768; DOI=10.4049/jimmunol.167.8.4430; RA Kawaguchi M., Onuchic L.F., Li X.-D., Essayan D.M., Schroeder J., RA Xiao H.-Q., Liu M.C., Krishnaswamy G., Germino G., Huang S.-K.; RT "Identification of a novel cytokine, ML-1, and its expression in subjects RT with asthma."; RL J. Immunol. 167:4430-4435(2001). RN [5] RP PROTEIN SEQUENCE OF 31-45. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [6] RP SUBUNIT. RX PubMed=17355969; DOI=10.1074/jbc.m700499200; RA Wright J.F., Guo Y., Quazi A., Luxenberg D.P., Bennett F., Ross J.F., RA Qiu Y., Whitters M.J., Tomkinson K.N., Dunussi-Joannopoulos K., RA Carreno B.M., Collins M., Wolfman N.M.; RT "Identification of an interleukin 17F/17A heterodimer in activated human RT CD4+ T cells."; RL J. Biol. Chem. 282:13447-13455(2007). RN [7] RP FUNCTION, AND INTERACTION WITH IL17RC. RX PubMed=17911633; DOI=10.4049/jimmunol.179.8.5462; RA Kuestner R.E., Taft D.W., Haran A., Brandt C.S., Brender T., Lum K., RA Harder B., Okada S., Ostrander C.D., Kreindler J.L., Aujla S.J., RA Reardon B., Moore M., Shea P., Schreckhise R., Bukowski T.R., Presnell S., RA Guerra-Lewis P., Parrish-Novak J., Ellsworth J.L., Jaspers S., Lewis K.E., RA Appleby M., Kolls J.K., Rixon M., West J.W., Gao Z., Levin S.D.; RT "Identification of the IL-17 receptor related molecule IL-17RC as the RT receptor for IL-17F."; RL J. Immunol. 179:5462-5473(2007). RN [8] RP FUNCTION, AND INTERACTION WITH IL17RA AND IL17RC. RX PubMed=18684971; DOI=10.4049/jimmunol.181.4.2799; RA Wright J.F., Bennett F., Li B., Brooks J., Luxenberg D.P., Whitters M.J., RA Tomkinson K.N., Fitz L.J., Wolfman N.M., Collins M., RA Dunussi-Joannopoulos K., Chatterjee-Kishore M., Carreno B.M.; RT "The human IL-17F/IL-17A heterodimeric cytokine signals through the IL- RT 17RA/IL-17RC receptor complex."; RL J. Immunol. 181:2799-2805(2008). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), AND FUNCTION. RX PubMed=11574464; DOI=10.1093/emboj/20.19.5332; RA Hymowitz S.G., Filvaroff E.H., Yin J.P., Lee J., Cai L., Risser P., RA Maruoka M., Mao W., Foster J., Kelley R.F., Pan G., Gurney A.L., RA de Vos A.M., Starovasnik M.A.; RT "IL-17s adopt a cystine knot fold: structure and activity of a novel RT cytokine, IL-17F, and implications for receptor binding."; RL EMBO J. 20:5332-5341(2001). RN [10] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 31-163 IN COMPLEX WITH IL17R, RP GLYCOSYLATION AT ASN-83, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=19838198; DOI=10.1038/ni.1813; RA Ely L.K., Fischer S., Garcia K.C.; RT "Structural basis of receptor sharing by interleukin 17 cytokines."; RL Nat. Immunol. 10:1245-1251(2009). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 31-163 IN COMPLEX WITH IL17A; RP INTERACTION WITH IL17RA AND IL17RC, FUNCTION, AND MUTAGENESIS OF ARG-77. RX PubMed=28827714; DOI=10.1038/s41598-017-08360-9; RA Goepfert A., Lehmann S., Wirth E., Rondeau J.M.; RT "The human IL-17A/F heterodimer: a two-faced cytokine with unique receptor RT recognition properties."; RL Sci. Rep. 7:8906-8906(2017). RN [12] RP X-RAY CRYSTALLOGRAPHY (3.32 ANGSTROMS) OF 31-163 IN COMPLEX WITH IL17RC, RP DISULFIDE BOND, INTERACTION WITH IL17A; IL17RC AND IL17RA, AND FUNCTION. RX PubMed=32187518; DOI=10.1016/j.immuni.2020.02.004; RA Goepfert A., Lehmann S., Blank J., Kolbinger F., Rondeau J.M.; RT "Structural Analysis Reveals that the Cytokine IL-17F Forms a Homodimeric RT Complex with Receptor IL-17RC to Drive IL-17RA-Independent Signaling."; RL Immunity 52:499-512.e5(2020). RN [13] RP VARIANT CANDF6 LEU-95, AND FUNCTION. RX PubMed=21350122; DOI=10.1126/science.1200439; RA Puel A., Cypowyj S., Bustamante J., Wright J.F., Liu L., Lim H.K., RA Migaud M., Israel L., Chrabieh M., Audry M., Gumbleton M., Toulon A., RA Bodemer C., El-Baghdadi J., Whitters M., Paradis T., Brooks J., Collins M., RA Wolfman N.M., Al-Muhsen S., Galicchio M., Abel L., Picard C., RA Casanova J.L.; RT "Chronic mucocutaneous candidiasis in humans with inborn errors of RT interleukin-17 immunity."; RL Science 332:65-68(2011). CC -!- FUNCTION: Effector cytokine of innate and adaptive immune system CC involved in antimicrobial host defense and maintenance of tissue CC integrity (PubMed:21350122). IL17A-IL17F signals via IL17RA-IL17RC CC heterodimeric receptor complex, triggering homotypic interaction of CC IL17RA and IL17RC chains with TRAF3IP2 adapter through SEFIR domains. CC This leads to downstream TRAF6-mediated activation of NF-kappa-B and CC MAPkinase pathways ultimately resulting in transcriptional activation CC of cytokines, chemokines, antimicrobial peptides and matrix CC metalloproteinases, with potential strong immune inflammation CC (PubMed:18684971, PubMed:21350122, PubMed:11591732, PubMed:11591768, CC PubMed:17911633, PubMed:11574464, PubMed:28827714). IL17A-IL17F is CC primarily involved in host defense against extracellular bacteria and CC fungi by inducing neutrophilic inflammation (By similarity). As CC signature effector cytokine of T-helper 17 cells (Th17), primarily CC induces neutrophil activation and recruitment at infection and CC inflammatory sites (By similarity). Stimulates the production of CC antimicrobial beta-defensins DEFB1, DEFB103A, and DEFB104A by mucosal CC epithelial cells, limiting the entry of microbes through the epithelial CC barriers (By similarity). IL17F homodimer can signal via IL17RC CC homodimeric receptor complex, triggering downstream activation of TRAF6 CC and NF-kappa-B signaling pathway (PubMed:32187518). Via IL17RC induces CC transcriptional activation of IL33, a potent cytokine that stimulates CC group 2 innate lymphoid cells and adaptive T-helper 2 cells involved in CC pulmonary allergic response to fungi. Likely via IL17RC, promotes CC sympathetic innervation of peripheral organs by coordinating the CC communication between gamma-delta T cells and parenchymal cells. CC Stimulates sympathetic innervation of thermogenic adipose tissue by CC driving TGFB1 expression (By similarity). Regulates the composition of CC intestinal microbiota and immune tolerance by inducing antimicrobial CC proteins that specifically control the growth of commensal Firmicutes CC and Bacteroidetes (By similarity). {ECO:0000250|UniProtKB:Q7TNI7, CC ECO:0000269|PubMed:11574464, ECO:0000269|PubMed:11591732, CC ECO:0000269|PubMed:11591768, ECO:0000269|PubMed:17911633, CC ECO:0000269|PubMed:18684971, ECO:0000269|PubMed:21350122, CC ECO:0000269|PubMed:28827714, ECO:0000269|PubMed:32187518}. CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:19838198, CC PubMed:32187518). Heterodimer with IL17A (IL17A-IL17F) CC (PubMed:17355969). Forms complexes with IL17RA and IL17RC receptors CC with 2:1 binding stoichiometry: two receptor chains for one interleukin CC molecule. IL17F homodimer forms predominantly complexes with IL17RC CC homodimer, whereas IL17A-IL17F favors complexes with IL17RA-IL17RC CC (PubMed:32187518, PubMed:28827714, PubMed:17911633, PubMed:18684971). CC IL17RA and IL17RC chains cannot distinguish between IL17A and IL17F CC molecules, potentially enabling the formation of topologically distinct CC complexes (PubMed:28827714). {ECO:0000269|PubMed:17355969, CC ECO:0000269|PubMed:17911633, ECO:0000269|PubMed:18684971, CC ECO:0000269|PubMed:19838198, ECO:0000269|PubMed:28827714, CC ECO:0000269|PubMed:32187518}. CC -!- INTERACTION: CC Q96PD4; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-10292310, EBI-10172181; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q7TNI7}. CC -!- TISSUE SPECIFICITY: Expressed in T-helper 1 and T-helper 2 cells, CC basophils and mast cells. {ECO:0000269|PubMed:11591768}. CC -!- DISEASE: Candidiasis, familial, 6 (CANDF6) [MIM:613956]: A primary CC immunodeficiency disorder with altered immune responses and impaired CC clearance of fungal infections, selective against Candida. It is CC characterized by persistent and/or recurrent infections of the skin, CC nails and mucous membranes caused by organisms of the genus Candida, CC mainly Candida albicans. {ECO:0000269|PubMed:21350122}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the IL-17 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL14427.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-17 entry; CC URL="https://en.wikipedia.org/wiki/Interleukin_17"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF384857; AAK83350.1; -; mRNA. DR EMBL; AL034343; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC070124; AAH70124.1; -; mRNA. DR EMBL; AF332389; AAL14427.1; ALT_SEQ; mRNA. DR CCDS; CCDS4938.1; -. DR RefSeq; NP_443104.1; NM_052872.3. DR RefSeq; XP_011512578.1; XM_011514276.1. DR PDB; 1JPY; X-ray; 2.85 A; A/B/X/Y=31-163. DR PDB; 3JVF; X-ray; 3.30 A; A/B=31-163. DR PDB; 5N92; X-ray; 2.30 A; F=31-163. DR PDB; 5NAN; X-ray; 3.30 A; E/F=31-163. DR PDB; 6HG4; X-ray; 3.32 A; A=31-163. DR PDB; 6HG9; X-ray; 3.62 A; A=31-163. DR PDB; 6HGO; X-ray; 2.10 A; A/B/C/D=31-163. DR PDB; 6PPG; X-ray; 2.75 A; F/G=31-163. DR PDBsum; 1JPY; -. DR PDBsum; 3JVF; -. DR PDBsum; 5N92; -. DR PDBsum; 5NAN; -. DR PDBsum; 6HG4; -. DR PDBsum; 6HG9; -. DR PDBsum; 6HGO; -. DR PDBsum; 6PPG; -. DR AlphaFoldDB; Q96PD4; -. DR SMR; Q96PD4; -. DR BioGRID; 125201; 32. DR IntAct; Q96PD4; 1. DR STRING; 9606.ENSP00000337432; -. DR BindingDB; Q96PD4; -. DR ChEMBL; CHEMBL4630880; -. DR DrugBank; DB12917; Bimekizumab. DR GlyCosmos; Q96PD4; 1 site, No reported glycans. DR GlyGen; Q96PD4; 1 site. DR iPTMnet; Q96PD4; -. DR PhosphoSitePlus; Q96PD4; -. DR BioMuta; IL17F; -. DR DMDM; 239938888; -. DR MassIVE; Q96PD4; -. DR PaxDb; 9606-ENSP00000337432; -. DR PeptideAtlas; Q96PD4; -. DR ProteomicsDB; 77668; -. DR ABCD; Q96PD4; 54 sequenced antibodies. DR Antibodypedia; 30885; 962 antibodies from 41 providers. DR DNASU; 112744; -. DR Ensembl; ENST00000336123.5; ENSP00000337432.4; ENSG00000112116.11. DR Ensembl; ENST00000699946.1; ENSP00000514702.1; ENSG00000112116.11. DR GeneID; 112744; -. DR KEGG; hsa:112744; -. DR MANE-Select; ENST00000336123.5; ENSP00000337432.4; NM_052872.4; NP_443104.1. DR UCSC; uc003pam.2; human. DR AGR; HGNC:16404; -. DR CTD; 112744; -. DR DisGeNET; 112744; -. DR GeneCards; IL17F; -. DR HGNC; HGNC:16404; IL17F. DR HPA; ENSG00000112116; Tissue enhanced (lymphoid). DR MalaCards; IL17F; -. DR MIM; 606496; gene. DR MIM; 613956; phenotype. DR neXtProt; NX_Q96PD4; -. DR OpenTargets; ENSG00000112116; -. DR Orphanet; 1334; Chronic mucocutaneous candidiasis. DR PharmGKB; PA29800; -. DR VEuPathDB; HostDB:ENSG00000112116; -. DR eggNOG; ENOG502S5A0; Eukaryota. DR GeneTree; ENSGT00940000156618; -. DR HOGENOM; CLU_118641_0_0_1; -. DR InParanoid; Q96PD4; -. DR OMA; SPWDYNV; -. DR OrthoDB; 5400717at2759; -. DR PhylomeDB; Q96PD4; -. DR TreeFam; TF314701; -. DR PathwayCommons; Q96PD4; -. DR Reactome; R-HSA-448424; Interleukin-17 signaling. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR SignaLink; Q96PD4; -. DR BioGRID-ORCS; 112744; 13 hits in 1134 CRISPR screens. DR EvolutionaryTrace; Q96PD4; -. DR GenomeRNAi; 112744; -. DR Pharos; Q96PD4; Tclin. DR PRO; PR:Q96PD4; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q96PD4; Protein. DR Bgee; ENSG00000112116; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 36 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW. DR GO; GO:0005125; F:cytokine activity; IDA:UniProtKB. DR GO; GO:0019955; F:cytokine binding; IDA:UniProtKB. DR GO; GO:0005126; F:cytokine receptor binding; IEA:Ensembl. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0051216; P:cartilage development; IDA:UniProtKB. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0097400; P:interleukin-17-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB. DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IEA:Ensembl. DR GO; GO:2000340; P:positive regulation of chemokine (C-X-C motif) ligand 1 production; IDA:UniProtKB. DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB. DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IEA:Ensembl. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB. DR GO; GO:0032761; P:positive regulation of lymphotoxin A production; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0032645; P:regulation of granulocyte macrophage colony-stimulating factor production; IDA:UniProtKB. DR GO; GO:0032663; P:regulation of interleukin-2 production; IDA:UniProtKB. DR GO; GO:0032675; P:regulation of interleukin-6 production; IDA:UniProtKB. DR GO; GO:0032677; P:regulation of interleukin-8 production; IDA:UniProtKB. DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB. DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1. DR InterPro; IPR029034; Cystine-knot_cytokine. DR InterPro; IPR020440; IL-17_chr. DR InterPro; IPR010345; IL-17_fam. DR Pfam; PF06083; IL17; 1. DR PRINTS; PR01932; INTRLEUKIN17. DR SUPFAM; SSF57501; Cystine-knot cytokines; 1. DR Genevisible; Q96PD4; HS. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Cytokine; Direct protein sequencing; KW Disease variant; Disulfide bond; Glycoprotein; Immunity; KW Inflammatory response; Innate immunity; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..30 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 31..163 FT /note="Interleukin-17F" FT /id="PRO_0000015432" FT CARBOHYD 83 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19838198" FT DISULFID 47 FT /note="Interchain (with C-137)" FT /evidence="ECO:0000269|PubMed:19838198" FT DISULFID 102..152 FT /evidence="ECO:0000269|PubMed:19838198, FT ECO:0000269|PubMed:32187518" FT DISULFID 107..154 FT /evidence="ECO:0000269|PubMed:19838198, FT ECO:0000269|PubMed:32187518" FT DISULFID 137 FT /note="Interchain (with C-47)" FT /evidence="ECO:0000269|PubMed:19838198" FT VARIANT 95 FT /note="S -> L (in CANDF6; dbSNP:rs748486078)" FT /evidence="ECO:0000269|PubMed:21350122" FT /id="VAR_065813" FT VARIANT 126 FT /note="E -> G (in dbSNP:rs2397084)" FT /id="VAR_058287" FT VARIANT 155 FT /note="V -> I (in dbSNP:rs11465553)" FT /id="VAR_058288" FT VARIANT 161 FT /note="H -> R (in dbSNP:rs763780)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_058289" FT MUTAGEN 77 FT /note="R->A: Significantly decreases the affinity for FT IL17RA and IL17RC by nearly 5-fold and 200-fold, FT respectively." FT /evidence="ECO:0000269|PubMed:28827714" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:1JPY" FT STRAND 55..62 FT /evidence="ECO:0007829|PDB:6HGO" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:6HGO" FT TURN 68..71 FT /evidence="ECO:0007829|PDB:5N92" FT HELIX 74..77 FT /evidence="ECO:0007829|PDB:6HGO" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:6HGO" FT STRAND 82..88 FT /evidence="ECO:0007829|PDB:6HGO" FT STRAND 92..103 FT /evidence="ECO:0007829|PDB:6HGO" FT STRAND 105..108 FT /evidence="ECO:0007829|PDB:6HGO" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:5N92" FT STRAND 118..134 FT /evidence="ECO:0007829|PDB:6HGO" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:6HGO" FT STRAND 140..155 FT /evidence="ECO:0007829|PDB:6HGO" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:3JVF" SQ SEQUENCE 163 AA; 18045 MW; E5287737C9E7BD46 CRC64; MTVKTLHGPA MVKYLLLSIL GLAFLSEAAA RKIPKVGHTF FQKPESCPPV PGGSMKLDIG IINENQRVSM SRNIESRSTS PWNYTVTWDP NRYPSEVVQA QCRNLGCINA QGKEDISMNS VPIQQETLVV RRKHQGCSVS FQLEKVLVTV GCTCVTPVIH HVQ //